ID F0VF65_NEOCL Unreviewed; 462 AA.
AC F0VF65;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN ORFNames=BN1204_021470 {ECO:0000313|EMBL:CEL66329.1}, BN1204_021480
GN {ECO:0000313|EMBL:CEL66330.1}, NCLIV_021470
GN {ECO:0000313|EMBL:CBZ52359.1}, NCLIV_021480
GN {ECO:0000313|EMBL:CBZ52360.1};
OS Neospora caninum (strain Liverpool).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ52359.1, ECO:0000313|Proteomes:UP000007494};
RN [1] {ECO:0000313|EMBL:CBZ52359.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:CBZ52359.1};
RA Aslett M.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBZ52359.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:CBZ52359.1};
RA Reid A.J., Sohal A., Harris D., Quail M., Sanders M., Berriman M.,
RA Wastling J.M., Pain A.;
RT "Comparative genomics and transcriptomics of Neospora caninum and
RT Toxoplasma gondii.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000007494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|Proteomes:UP000007494};
RX PubMed=22457617; DOI=10.1371/journal.ppat.1002567;
RA Reid A.J., Vermont S.J., Cotton J.A., Harris D., Hill-Cawthorne G.A.,
RA Konen-Waisman S., Latham S.M., Mourier T., Norton R., Quail M.A.,
RA Sanders M., Shanmugam D., Sohal A., Wasmuth J.D., Brunk B., Grigg M.E.,
RA Howard J.C., Parkinson J., Roos D.S., Trees A.J., Berriman M., Pain A.,
RA Wastling J.M.;
RT "Comparative genomics of the apicomplexan parasites Toxoplasma gondii and
RT Neospora caninum: Coccidia differing in host range and transmission
RT strategy.";
RL PLoS Pathog. 8:e1002567-e1002567(2012).
RN [4] {ECO:0000313|EMBL:CEL66329.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:CEL66329.1};
RX PubMed=25875305; DOI=10.1371/journal.pone.0124473;
RA Ramaprasad A., Mourier T., Naeem R., Malas T.B., Moussa E., Panigrahi A.,
RA Vermont S.J., Otto T.D., Wastling J., Pain A.;
RT "Comprehensive Evaluation of Toxoplasma gondii VEG and Neospora caninum LIV
RT Genomes with Tachyzoite Stage Transcriptome and Proteome Defines Novel
RT Transcript Features.";
RL PLoS ONE 10:e0124473-e0124473(2015).
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689}.
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DR EMBL; FR823388; CBZ52359.1; -; Genomic_DNA.
DR EMBL; FR823388; CBZ52360.1; -; Genomic_DNA.
DR EMBL; LN714481; CEL66329.1; -; Genomic_DNA.
DR EMBL; LN714481; CEL66330.1; -; Genomic_DNA.
DR RefSeq; XP_003882391.1; XM_003882342.1.
DR RefSeq; XP_003882392.1; XM_003882343.1.
DR AlphaFoldDB; F0VF65; -.
DR GeneID; 13444281; -.
DR GeneID; 13444282; -.
DR VEuPathDB; ToxoDB:NCLIV_021470; -.
DR VEuPathDB; ToxoDB:NCLIV_021480; -.
DR eggNOG; ENOG502QQ0A; Eukaryota.
DR InParanoid; F0VF65; -.
DR OrthoDB; 313696at2759; -.
DR Proteomes; UP000007494; Chromosome VIIa.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IEA:InterPro.
DR GO; GO:0042853; P:L-alanine catabolic process; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
DR CDD; cd05305; L-AlaDH; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR008141; Ala_DH.
DR InterPro; IPR008143; Ala_DH/PNT_CS2.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR026255; NADP_transhyd_a.
DR PANTHER; PTHR42795; ALANINE DEHYDROGENASE; 1.
DR PANTHER; PTHR42795:SF1; ALANINE DEHYDROGENASE 1; 1.
DR Pfam; PF01262; AlaDh_PNT_C; 2.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR PIRSF; PIRSF000203; NADP_transhydrogenase_alpha; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00837; ALADH_PNT_2; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007494}.
FT DOMAIN 31..164
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 176..345
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 462 AA; 50051 MW; A669009A3C7BA940 CRC64;
MAPTTTKMAS LTSQLRFSTP ATAVTETCTI GCPKEVMPCE YRVSLTPATV AELVSNGHTV
VVQMGAGVAS GFTDESYTAS GATVVPTAKE VYTTCQTIVK VQAPQPQEYS FIQQGQVIFA
FFSFENNKTL FETMMQREAV CFSYEHMKTE NGMTPVLQAM CEISGQLAIS QAMKYLEKPM
GGSGCMLGTV TGMTSGYVLI LGGGVAAMQA ARVASSVGAH VCVMDVCMSN LRTMAETFPK
NCTTLYFCTE NLVQEIQKAD VVIGAVFGSF QMPSTVTNSS VMSEMTTVNQ MNRAPILVTK
EQVAMMKPGS VIVDLAASRG GNFETTQPTT LEMPTFMYNN VIHYCVPNMP SAVPQTSSVS
LANNTLVYIQ QVANNGWKKA CVENSTLMQG LMVAQNMTTN YTLSQIYTGT MFVPTVQLLK
NEITMMTTQP QNQTETTLAE IKQQLNQIQN MNSTYGNFTV EA
//
